Evidence map›Paper›PMID 33398331›Full record

ArticleNucleic acids research2021

Arabidopsis mTERF9 protein promotes chloroplast ribosomal assembly and translation by establishing ribonucleoprotein interactions in vivo.

Louis-Valentin Méteignier, Rabea Ghandour, Aude Zimmerman, Lauriane Kuhn, Jörg Meurer, Reimo Zoschke, Kamel Hammani

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.3field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
  2. Alphafuser: a parsimonious approach to predicting higher-order protein complexes.Acta crystallographica. Section D, Structural biology · 2026
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  8. Review
  9. Light response of gametophyte inFrontiers in plant science · 2023
    Article
  10. GTPase Era at the heart of ribosome assembly.Frontiers in molecular biosciences · 2023
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 2 countries.

Louis-Valentin MéteignierInstitut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg, 12 rue du Général Zimmer, 67084 Strasbourg, France.
Rabea GhandourMax Planck Institute of Molecular Plant Physiology, Am Mühlenberg 1, 14476 Potsdam-Golm, Germany.
Aude ZimmermanInstitut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg, 12 rue du Général Zimmer, 67084 Strasbourg, France.
Lauriane KuhnPlateforme protéomique Strasbourg Esplanade FRC1589 du CNRS, Université de Strasbourg, 15 rue René Descartes, 67084 Strasbourg, France.
Jörg MeurerPlant Sciences, Faculty of Biology, Ludwig-Maximilians-University Munich, Großhaderner Street 2-4, 82152 Planegg-Martinsried, Germany.
Reimo ZoschkeMax Planck Institute of Molecular Plant Physiology, Am Mühlenberg 1, 14476 Potsdam-Golm, Germany.
Kamel HammaniInstitut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg, 12 rue du Général Zimmer, 67084 Strasbourg, France.
Centre National de la Recherche Scientifique · FRMax Planck Institute of Molecular Plant Physiology · DELudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mitochondrial transcription termination factor proteins are nuclear-encoded nucleic acid binders defined by degenerate tandem helical-repeats of ∼30 amino acids. They are found in metazoans and plants where they localize in organelles. In higher plants, the mTERF family comprises ∼30 members and several of these have been linked to plant development and response to abiotic stress. However, knowledge of the molecular basis underlying these physiological effects is scarce. We show that the Arabidopsis mTERF9 protein promotes the accumulation of the 16S and 23S rRNAs in chloroplasts, and interacts predominantly with the 16S rRNA in vivo and in vitro. Furthermore, mTERF9 is found in large complexes containing ribosomes and polysomes in chloroplasts. The comprehensive analysis of mTERF9 in vivo protein interactome identified many subunits of the 70S ribosome whose assembly is compromised in the null mterf9 mutant, putative ribosome biogenesis factors and CPN60 chaperonins. Protein interaction assays in yeast revealed that mTERF9 directly interact with these proteins. Our data demonstrate that mTERF9 integrates protein-protein and protein-RNA interactions to promote chloroplast ribosomal assembly and translation. Besides extending our knowledge of mTERF functional repertoire in plants, these findings provide an important insight into the chloroplast ribosome biogenesis.

Indexed as

Organelle BiogenesisArabidopsisArabidopsis ProteinsChloroplast ProteinsChloroplastsGene Expression Regulation, PlantPeptide Termination FactorsPolyribosomesProtein BiosynthesisRecombinant ProteinsRibonucleoproteinsRibosomesRNA, PlantRNA, Ribosomal, 16SRNA, Ribosomal, 23SSubstrate SpecificityArabidopsis ProteinsChloroplast ProteinsERA1 protein, ArabidopsisMTERF9 protein, ArabidopsisPeptide Termination FactorsRecombinant ProteinsRibonucleoproteinsRNA, PlantRNA, Ribosomal, 16SRNA, Ribosomal, 23S

Identifiers

PMID33398331
PMCPMC7826268
OpenAlexW3118714830

What Socratic holds

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LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.